Our long range objective is to determine the three-dimensional structures of biologically and medically relevant proteins of the vascular system. These proteins are involved in the transport and recycling of vital raw materials in the body. X-ray crystallographic techniques will be applied to the hemoglobin-haptoglobin complex. Crystals have already been obtained and unit cell parameters will be determined. Heavy atom derivatives will be prepared and solved by utilizing our knowledge of hemoglobin. Electron density maps will be calculated showing the structure of the complex, the interaction sites of the two proteins, and any modifications in the confirmation of the hemoglobin molecule. The structure will provide new evidence about the function of haptoglobin and may help explain the elevated haptoglobin levels in heart disorders and cancers. Taking advantage of the known structure of hemoglobin, Patterson search techniques and direct methods will be tried on the complex in order to develop new methods of solving protein crystal structures. An automated system for interpreting protein electron density maps is being developed using pattern recognition methods. Such a system will allow the crystallographer to interpret his maps very quickly and thus be able to correlate the structure with the functionally and clinically important properties very much faster. We are attempting to crystallize other blood proteins, including erythrocyte glycoprotein, the site of all blood group antigens, transferrin and oeruloplasmin, iron and copper binding proteins in the serum.